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Article

The crystal structure of chorismate lyase shows a new fold and a tightly retained product.

Proteins - 15 Aug 2001

Gallagher D T, Mayhew M, Holden M J, Howard A, Kim K J, Vilker V L

Abstract excerpt

The enzyme chorismate lyase (CL) catalyzes the removal of pyruvate from chorismate to produce 4-hydroxy benzoate (4HB) for the ubiquinone pathway. In Escherichia coli, CL is monomeric, with 164 residues. We have determined the structure of the CL product complex by crystallographic heavy-atom methods and report the structure at 1.4-A resolution for a fully active double Cys-to-Ser mutant and at 2.0-A resolution...

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Identifiers

PMID: 11455603
DOI: 10.1002/prot.1095

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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